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Literature summary for 2.4.1.12 extracted from

  • Morgan, J.L.W.; Strumillo, J.; Zimmer, J.
    Crystallographic snapshot of cellulose synthesis and membrane translocation (2013), Nature, 493, 181-186.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
cyclic-di-GMP BcsA contains a PilZ domain within its C-terminal, intracellular domain and its activity is strongly stimulated by the bacterial secondary messenger cyclic-di-GMP Cereibacter sphaeroides

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43 Cereibacter sphaeroides

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant native and selenomethionine -labeled complex of BcsA and BcsB containing a translocating polysaccharide, from 30% PEG 200, 0.1 M MES, pH 6.5, and 50 mM NaCl at 4°C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview Cereibacter sphaeroides

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane cellulose synthases are membrane-embedded glycosyltransferases. BcsB is a periplasmic protein that is anchored to the inner membrane via a single, C-terminal transmembrane helix. BcsA and BcsB are fused Cereibacter sphaeroides
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucose + [(1->4)-beta-D-glucosyl]n Cereibacter sphaeroides
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UDP + [(1->4)-beta-D-glucosyl]n+1
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?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides Q3J125
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged native and selenomethionine -labeled subunits BcsA and B from Escherichia coli strain C43 by nickel affinity chromatography and gel filtration Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucose + [(1->4)-beta-D-glucosyl]n
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Cereibacter sphaeroides UDP + [(1->4)-beta-D-glucosyl]n+1
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?

Subunits

Subunits Comment Organism
dimer BcsA and BcsB form a 1:1 stoichiometric complex spanning approximately 150 A perpendicular and 55 A parallel to the membrane. The complex is divided into a cuboid-shaped membrane-spanning region sandwiched between large cytoplasmic and periplasmic domains. BcsA contains four N-terminal and four C-terminal transmembrane-helices separated by a large intracellular loop (4/5-loop) that forms a GT-domain (aa 128 to 368). transmembrane domains 3-8 form a narrow channel for the translocating polysaccharide and BcsA's intracellular C-terminus (aa 575 to 759) contains a 6-stranded beta-barrel and a highly curved alpha-helical region that attaches the beta-barrel to the GT-domain. BcsB is a dome-shaped, beta-strand rich, periplasmic protein. Its N-terminal region forms the tip of the dome, whereas the C-terminal transmembrane-anchor interacts with BcsA. Two amphipathic helices further stabilize its interaction with BcsA and the periplasmic water-membrane interface. Domain structures. Modeling, overview Cereibacter sphaeroides

Synonyms

Synonyms Comment Organism
BcsA-B
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Cereibacter sphaeroides
inner membrane-associated bacterial cellulose synthase
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Cereibacter sphaeroides

General Information

General Information Comment Organism
additional information structure of the BcsA-B translocation intermediate revealing the architecture of the cellulose synthase. Subunit BcsA forms a cellulose-conducting channel, modeling for the coupling of cellulose synthesis and translocation in which the nascent polysaccharide is extended by one glucose molecule at a time, overview Cereibacter sphaeroides
physiological function cellulose synthases (CESAs) are membrane-embedded glycosyltransferases, which utilize UDP-activated glucose (UDP-Glc) to processively elongate the nascent polysaccharide in a reaction that inverts the configuration at the anomeric carbon of the newly added sugar from alpha to beta. Cellulose synthesis and transport across the inner bacterial membrane is mediated by a complex of the multi-spanning catalytic BcsA subunit and the membrane-anchored, periplasmic BcsB protein. Structure-function analysis and modeling, overview Cereibacter sphaeroides